GHRHR_PIG
ID GHRHR_PIG Reviewed; 423 AA.
AC P34999; Q28993;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Growth hormone-releasing hormone receptor;
DE Short=GHRH receptor;
DE AltName: Full=Growth hormone-releasing factor receptor;
DE Short=GRF receptor;
DE Short=GRFR;
DE Flags: Precursor;
GN Name=GHRHR;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=8413847; DOI=10.1016/0143-4179(93)90062-f;
RA Hsiung H.M., Smith D.P., Zhang X.-Y., Bennett T., Rosteck P.R. Jr.,
RA Lai M.-H.;
RT "Structure and functional expression of a complementary DNA for porcine
RT growth hormone-releasing hormone receptor.";
RL Neuropeptides 25:1-10(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hazem H.A., Zhang X., Smith D.P., Heiman M.L., Hsiung H.M.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for GRF, coupled to G proteins which activate
CC adenylyl cyclase. Stimulates somatotroph cell growth, growth hormone
CC gene transcription and growth hormone secretion.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Pituitary gland. Also detected in the lymphocytes
CC and thymocytes.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; L11869; AAA31047.1; -; mRNA.
DR EMBL; U49435; AAA93391.1; -; mRNA.
DR PIR; I46586; I46586.
DR RefSeq; NP_999200.1; NM_214035.2.
DR AlphaFoldDB; P34999; -.
DR SMR; P34999; -.
DR STRING; 9823.ENSSSCP00000017661; -.
DR PaxDb; P34999; -.
DR PRIDE; P34999; -.
DR GeneID; 397100; -.
DR KEGG; ssc:397100; -.
DR CTD; 2692; -.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; P34999; -.
DR OMA; RFYIELC; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR GO; GO:0016520; F:growth hormone-releasing hormone receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR003288; GPCR_2_GHRH_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR PANTHER; PTHR45620:SF14; PTHR45620:SF14; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR01352; GHRHRECEPTOR.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..423
FT /note="Growth hormone-releasing hormone receptor"
FT /id="PRO_0000012830"
FT TOPO_DOM 23..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..357
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..64
FT /evidence="ECO:0000250"
FT DISULFID 55..96
FT /evidence="ECO:0000250"
FT DISULFID 78..112
FT /evidence="ECO:0000250"
FT CONFLICT 419..423
FT /note="LTTVC -> SACSRAGSSRPRAHGDTYPGLEVPGQWLCLFLT (in Ref.
FT 1; AAA31047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 47200 MW; 6768357DCB4AD603 CRC64;
MDSGVWAACI FCLLSSLPVA LGHVHPECDF ITQLREDERT CLQAADRMAN SSSGCPRTWD
GLLCWPTAGP GEWVTLPCPA FFSHFSSEPG ALKRDCTTTG WSEPFPPYPE ACPVPLELLT
DEKSYFSTVR IVYTTGHSVS AVALFVAIAI LVALRRLHCP RNYIHSQLFA TFILKAGAVF
LKDAALFHSE NTDHCSFSTV LCKVSVATSH FATMTNFSWL LAEAVYLTCL LASTSPSTRR
AFWWLVLAGW GLPLLFTGTW VGCKLAFEDV ACWDLDDSSP YWWIIKGPIV LSVGVNFGLF
LNIIRILLRK LEPAQGSLHT QPQYWRLSKS TLLLIPLFGI HYVIFNFLPD SAGLGIRLPL
ELGLGSFQGF IVAILYCFLN QEVRTEISRR WHGHDPELLP AWRTHAKWAK PSRSRAKVLT
TVC
